Recombinant Mouse Anti-Shigella flexneri variant Y Antibody Fab Fragment (SYA/J6) (CAT#: PABX-171-F (E))

Anti-Shigella flexneri variant Y antibody is a Mouse of Fab class that binds to an Shigella flexneri variant Y. The antibody binds an optimal trisaccharide epitope, a residue sequence BCD of the ABCD [f2)-R-L-Rha- (1f2)-R-L-Rha- (1f3)-R-L-Rha- (1f3)-â-D-GlcNAc- (1f] repeating unit of the O-polysaccharide of the S. flexneri variant Y LPS.

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  • Published Data
  • Datasheet
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Figure 1 (Φ,Ψ) maps of the trajectories for the glycosidic linkages of 3RU segments of O-Ags Y and 2a.

Squares and stars indicate the bound conformations of ABCDA' pentasaccharide and deoxygenated BC*D to mAb SYA/J6, respectively. Circles and diamonds indicate the bound conformations of the nonreducing RU and middle RU of the synthetic [AB(E)CD]3 pentadecasaccharide to mAb F22-4, respectively.

Theillet, F. X., Simenel, C., Guerreiro, C., Phalipon, A., Mulard, L. A., & Delepierre, M. (2010). Effects of backbone substitutions on the conformational behavior of Shigella flexneri O-antigens: implications for vaccine strategy. Glycobiology, 21(1), 109-121.

Figure 2 Structure of the Fab fragment of the SYA/J6 antibody with bound octapeptide.

(A) Stereoview of the backbone trace with the octapeptide bound in the groove between the two variable domains (VL and VH). The CDRs of the light (L) chain and the heavy (H) chain are: L1 and H1 (green), L2 and H2 (gray), and L3 and H3 (yellow). VL and VH framework regions are in blue and mauve, respectively. The N terminus of the peptide is located at the ''lower end'' of the groove. The atom types for the peptide are: C, green; N, blue; O, red; and S, yellow. (B) Electrostatic surface potential (10 kT, red; neutral, white; 10 kT blue) of the same structure shown in A. Also shown are three water molecules (white spheres, in the order S2, S9, and S1 from top to bottom) lodged in the pocket in the deepest part of the groove (see also Fig. 2B). (C) Similar to B, but with bound pentasaccharide (sugar residues in the order Rha A, Rha B, Rha C, GlcNAc D, and Rha A from top to bottom) (data from ref. 11). The atom types for the sugar are: C, yellow; N, blue; and O, red. Rha C mainly occupies the groove pocket.

Vyas, N. K., Vyas, M. N., Chervenak, M. C., Bundle, D. R., Pinto, B. M., & Quiocho, F. A. (2003). Structural basis of peptide–carbohydrate mimicry in an antibody-combining site. Proceedings of the National Academy of Sciences, 100(25), 15023-15028.


  • Immunogen
  • bacterial cells of Shigella flexneri variant Y
  • Host Species
  • Mouse
  • Derivation
  • Mouse
  • Type
  • Fab
  • Specificity
  • Tested positive against native Shigella flexneri variant Y
  • Species Reactivity
  • Shigella flexneri variant Y
  • Clone
  • SYA/J6
  • Applications
  • WB 1:1000-1:5000
    ELISA 1:10000-1:20000
    FuncS (assay dependent)


  • Application Notes
  • Assay-depended

For research use only. Not intended for any clinical use. No products from Creative Biolabs may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative Biolabs.

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* Abbreviations
3D IHC3D Immunohistochemistry
Cell ScreeningCell Screening
SeparationCell Separation
ChIPChromatin Immunoprecipitation
CMCDComplement Mediated Cell Depletion
DBDot Blot
EMElectron Microscopy
ELISAEnzyme-linked Immunosorbent Assay
ELISPOTEnzyme-linked Immunosorbent Spot
FCFlow Cytometry
FuncSFunctional Assay
GSGel Super Shift Assay
REImmunohistology - Resin Sections
IRMAImmunoradiometric Assay
SHIn situ hybridization
ICFCIntracellular Staining for Flow Cytometry
KO/KD-WBKnockout/Knockdown target confirmation by Western Blot
Live cell imagingLive cell imaging
CyTOF®Mass Cytometry
MeDIPMethylated DNA Immunoprecipitation
MultiplexMultiplex bead-based assay
PPProtein Purification
RIRadial Immunodiffusion
SPRSurface Plasmon Resonance
TCTissue Culture
WBWestern Blot

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